BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18045

Title: 1H,13C, and 15N chemical shift assignments for human endothelial monocyte-activating polypeptide II   PubMed: 22392337

Deposition date: 2011-11-07 Original release date: 2012-03-09

Authors: Lozhko, Dmytro; Stanek, Jan; Kazimierczuk, Krzysztof; Zawadzka-Kazimierczuk, Anna; Kozminski, Wiktor; Zhukov, Igor; Kornelyuk, Olexander

Citation: Lozhko, Dmytro; Stanek, Jan; Kazimierczuk, Krzysztof; Zawadzka-Kazimierczuk, Anna; Kozminski, Wiktor; Zhukov, Igor; Kornelyuk, Alexander. "(1)H, (13)C, and (15)N chemical shifts assignments for human endothelial monocyte-activating polypeptide EMAP II."  Biomol. NMR Assignments 7, 25-29 (2013).

Assembly members:
emap_II, polymer, 169 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
emap_II: AMDSKPIDVSRLDLRIGCII TARKHPDADSLYVEEVDVGE IAPRTVVSGLVNHVPLEQMQ NRMVILLCNLKPAKMRGVLS QAMVMCASSPEKIEILAPPN GSVPGDRITFDAFPGEPDKE LNPKKKIWEQIQPDLHTNDE CVATYKGVPFEVKGKGVCRA QTMSNSGIK

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts139
1H chemical shifts1104

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1emap II1

Entities:

Entity 1, emap II 169 residues - Formula weight is not available

two residues on N-termini Ala-Met are non-native

1   ALAMETASPSERLYSPROILEASPVALSER
2   ARGLEUASPLEUARGILEGLYCYSILEILE
3   THRALAARGLYSHISPROASPALAASPSER
4   LEUTYRVALGLUGLUVALASPVALGLYGLU
5   ILEALAPROARGTHRVALVALSERGLYLEU
6   VALASNHISVALPROLEUGLUGLNMETGLN
7   ASNARGMETVALILELEULEUCYSASNLEU
8   LYSPROALALYSMETARGGLYVALLEUSER
9   GLNALAMETVALMETCYSALASERSERPRO
10   GLULYSILEGLUILELEUALAPROPROASN
11   GLYSERVALPROGLYASPARGILETHRPHE
12   ASPALAPHEPROGLYGLUPROASPLYSGLU
13   LEUASNPROLYSLYSLYSILETRPGLUGLN
14   ILEGLNPROASPLEUHISTHRASNASPGLU
15   CYSVALALATHRTYRLYSGLYVALPROPHE
16   GLUVALLYSGLYLYSGLYVALCYSARGALA
17   GLNTHRMETSERASNSERGLYILELYS

Samples:

sample_1: emap II, [U-98% 13C; U-98% 15N], 0.7 mM; H2O 90%; D2O 10%; NaCl 250 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 8.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
4D HNCOCA random samplingsample_1isotropicsample_conditions_1
4D HNCACO random samplingsample_1isotropicsample_conditions_1
4D HCCH-TOCSY random samplingsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

Reconstruction_4D, Stanek J., Kozminski W. - processing

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz
  • Varian Uniform NMR System 700 MHz

Related Database Links:

PDB
DBJ BAE90551 BAG53174 BAG60265 BAG64889
EMBL CAA69993 CAG47076 CAH92571
GB AAA62202 AAH14051 AAX36997 ABM84225 ABM87736
REF NP_001126507 NP_001135887 NP_001135888 NP_004748 XP_001083775
SP Q12904

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts